Current Protein Identity:P01011 New Search
Main Difference Dimensions in This Set
Different construct Different mutation/modification Different assembly state Different ligand/ion Different experimental method Different experimental conditions Different structure-quality metrics

Difference tags compare only the current result set; every original PDB and assembly record remains separate.

Related-Structure Differences

Each row represents one biological assembly in one PDB entry; multiple monomers of the same protein are listed separately.

PDB Entry Assembly / Oligomeric State Construct Mutations and Modifications Ligands, Ions and Non-polymers Experimental Method Experimental Conditions Structure Quality
1AS4 CLEAVED ANTICHYMOTRYPSIN A349R Deposited 1997-08-12 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 43–383(341 aa) Fragment:CHAIN A CONTAINS RESIDUES 20 - 358, CHAIN B CONTAINS RESIDUES 359 - 393
Chain B 387–423(37 aa) Fragment:CHAIN A CONTAINS RESIDUES 20 - 358, CHAIN B CONTAINS RESIDUES 359 - 393
Mutation:A349R Mutation:A349R ACT ACETATE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.6;14% PEG MONOMETHYLETHER 5000, 0.2 M MAGNESIUM ACETATE 0.1 M SODIUM ACETATE PH 5.6 PROTEIN AT 3 MG/ML
Resolution 2.10 Å R-free 0.240
1QMN Alpha1-antichymotrypsin serpin in the delta conformation (partial loop insertion) Deposited 1999-10-04 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 26–423(398 aa)
Mutation:YES No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 4.5;291 K;1 MICROLITER OF 10MG/ML PROTEIN IN 50MM TRIS, 50MM KCL, PH 7.4 WAS MIXED WITH 2 MICROLITER OF PRECIPITANT AND EQUILIBRATED AS A HANGING DROP OVER 1ML OF PRECIPITANT (20% [W/V] PEG 4000, 0.2M AMMONIUM SULPHATE, 0.1M NAOAC, PH 4.5), AT 18 DEGREES C
Resolution 2.27 Å R-free 0.243
2ACH CRYSTAL STRUCTURE OF CLEAVED HUMAN ALPHA1-ANTICHYMOTRYPSIN AT 2.7 ANGSTROMS RESOLUTION AND ITS COMPARISON WITH OTHER SERPINS Deposited 1993-04-26 Assembly 1 Other combination Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 24–383(360 aa)
Chain B 384–423(40 aa)
Not recorded PO4 PHOSPHATE ION × 1 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.70 Å
2ACH CRYSTAL STRUCTURE OF CLEAVED HUMAN ALPHA1-ANTICHYMOTRYPSIN AT 2.7 ANGSTROMS RESOLUTION AND ITS COMPARISON WITH OTHER SERPINS Deposited 1993-04-26 Assembly 2 Other combination Homooligomer;Protein × 4 PDB declaration: tetrameric(4) Consistent with protein count
Chain A 24–383(360 aa)
Chain B 384–423(40 aa)
Not recorded PO4 PHOSPHATE ION × 2 X-RAY DIFFRACTION mmCIF provides none of the parsed conditions Resolution 2.70 Å
3CAA CLEAVED ANTICHYMOTRYPSIN A347R Deposited 1997-08-18 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 43–383(341 aa)
Chain B 387–423(37 aa)
Mutation:A347R Mutation:A347R No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.6;10% PEG MONOMETHYLETHER 5000 0.2 M MAGNESIUM ACETATE 0.1 M SODIUM CITRATE PH 5.6 PROTEIN AT 3 MG/ML
Resolution 2.40 Å R-free 0.280
3DLW Antichymotrypsin Deposited 2008-06-29 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 25–423(399 aa)
Mutation:A351G, A352T, V370T No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;pH 7.5;294 K;PEG 10,000, HEPES buffer, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 294K
Resolution 2.70 Å R-free 0.286
4CAA CLEAVED ANTICHYMOTRYPSIN T345R Deposited 1997-08-14 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 43–383(341 aa)
Chain B 387–423(37 aa)
Mutation:T345R Mutation:T345R No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions pH 5.6;14% PEG 8000 0.2 M MAGNESIUM ACETATE 0.1 M SODIUM CITRATE PH 5.6
Resolution 2.90 Å R-free 0.284
5OM2 Crystal structure of Alpha1-antichymotrypsin variant DBS-I1: a drug-binding serpin for doxycycline Deposited 2017-07-28 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 26–383(358 aa)
Chain B 384–423(40 aa)
Mutation:;L24R W194F W215Y E242Q K244N L269S P270Q K274A W276F R277F V355L K356E I357V T358L L359F L360Q S361G A362P P382D T383H D384F Q386W N387S ; Mutation:;L24R W194F W215Y E242Q K244N L269S P270Q K274A W276F R277F V355L K356E I357V T358L L359F L360Q S361G A362P P382D T383H D384F Q386W N387S ; EDO 1,2-ETHANEDIOL × 1 DXT (4S,4AR,5S,5AR,6R,12AS)-4-(DIMETHYLAMINO)-3,5,10,12,12A-PENTAHYDROXY-6-METHYL-1,11-DIOXO-1,4,4A,5,5A,6,11,12A-OCTAHYDROTETRACENE-2-CARBOXAMIDE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;293 K;0.2 M ammonium chloride, 20 % w/v PEG 3350
Resolution 1.47 Å R-free 0.202
5OM3 Crystal structure of Alpha1-antichymotrypsin variant DBS-I5: a MMP14-cleavable drug-binding serpin for doxycycline Deposited 2017-07-28 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 26–383(358 aa)
Chain B 384–423(40 aa)
Mutation:L24R W194F W215Y E242Q K244N L269S P270Q K274S W276F R277F V355L K356F T358P L360S S361L A362R L363M P382D T383H D384F Q386W N387S Mutation:L24R W194F W215Y E242Q K244N L269S P270Q K274S W276F R277F V355L K356F T358P L360S S361L A362R L363M P382D T383H D384F Q386W N387S PEG DI(HYDROXYETHYL)ETHER × 1 DXT (4S,4AR,5S,5AR,6R,12AS)-4-(DIMETHYLAMINO)-3,5,10,12,12A-PENTAHYDROXY-6-METHYL-1,11-DIOXO-1,4,4A,5,5A,6,11,12A-OCTAHYDROTETRACENE-2-CARBOXAMIDE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;293 K;0.2 M ammonium sulfate, 0.1 M BIS-TRIS pH 5.5, 25 % w/v PEG 3350
Resolution 2.00 Å R-free 0.219
5OM5 Crystal structure of Alpha1-antichymotrypsin variant DBS-I-allo1: an allosterically triggered drug-binding serpin for doxycycline Deposited 2017-07-28 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 26–383(358 aa)
Chain B 384–423(40 aa)
Mutation:;L24R W194F W215Y E242Q K244N L269S P270Q K274S W276F R277F A349R V355L K356E I357V T358L L359F L360Q S361G A362P P382D T383H D384F Q386W N387S ; Mutation:;L24R W194F W215Y E242Q K244N L269S P270Q K274S W276F R277F A349R V355L K356E I357V T358L L359F L360Q S361G A362P P382D T383H D384F Q386W N387S ; EDO 1,2-ETHANEDIOL × 3 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;293 K;0.1 M HEPES pH 7.0, 30 % v/v Jeffamine ED-2001 pH 7.0
Resolution 1.59 Å R-free 0.196
5OM6 Crystal structure of Alpha1-antichymotrypsin variant DBS-I-allo2: a MMP9-cleavable drug-binding serpin for doxycycline Deposited 2017-07-28 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 26–383(358 aa) Fragment:UNP residues 36-383
Chain B 384–423(40 aa) Fragment:UNP residues 384-423
Mutation:L24R W194F W215Y E242Q K244N L269S P270Q K274S W276F R277F A349R V355L I357G T358P L359R L360Q Mutation:L24R W194F W215Y E242Q K244N L269S P270Q K274S W276F R277F A349R V355L I357G T358P L359R L360Q CIT CITRIC ACID × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;293 K;0.1 M citric acid pH 3.5, 25 % w/v PEG 3350
Resolution 1.85 Å R-free 0.238
5OM6 Crystal structure of Alpha1-antichymotrypsin variant DBS-I-allo2: a MMP9-cleavable drug-binding serpin for doxycycline Deposited 2017-07-28 Assembly 2 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain C 26–383(358 aa) Fragment:UNP residues 36-383
Chain D 384–423(40 aa) Fragment:UNP residues 384-423
Mutation:L24R W194F W215Y E242Q K244N L269S P270Q K274S W276F R277F A349R V355L I357G T358P L359R L360Q Mutation:L24R W194F W215Y E242Q K244N L269S P270Q K274S W276F R277F A349R V355L I357G T358P L359R L360Q CIT CITRIC ACID × 1 EDO 1,2-ETHANEDIOL × 1 CL CHLORIDE ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;293 K;0.1 M citric acid pH 3.5, 25 % w/v PEG 3350
Resolution 1.85 Å R-free 0.238
5OM7 Crystal structure of Alpha1-antichymotrypsin variant DBS-II: a drug-binding serpin for doxorubicin Deposited 2017-07-28 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 26–383(358 aa)
Chain B 384–423(40 aa)
Mutation:;L24R W194F W215Y E242Q K244N L269S P270Q K274S W276F R277F D278E V355L K356E I357V T358L L359F L360Q S361G A362P P382D T383N D384F Q386W N387S ; Mutation:;L24R W194F W215Y E242Q K244N L269S P270Q K274S W276F R277F D278E V355L K356E I357V T358L L359F L360Q S361G A362P P382D T383N D384F Q386W N387S ; DM2 DOXORUBICIN × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;293 K;0.2 M ammonium chloride, 20 % w/v PEG 3350
Resolution 1.73 Å R-free 0.235
5OM8 Crystal form 2 of Alpha1-antichymotrypsin variant DBS-II-allo: an allosterically modulated drug-binding serpin for doxorubicin Deposited 2017-07-28 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 26–383(358 aa)
Chain B 384–423(40 aa)
Mutation:;L24R W194F W215Y E242Q K244N L269S P270Q K274S W276F R277F D278E A349R V355L K356E I357V T358L L359F L360Q S361G A362P P382D T383N D384F Q386W N387S ; Mutation:;L24R W194F W215Y E242Q K244N L269S P270Q K274S W276F R277F D278E A349R V355L K356E I357V T358L L359F L360Q S361G A362P P382D T383N D384F Q386W N387S ; CL CHLORIDE ION × 1 EDO 1,2-ETHANEDIOL × 1 NI NICKEL (II) ION × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;293 K;0.2 M Ammonium chloride, 20% w/v PEG 3350
Resolution 2.20 Å R-free 0.242
6FTP Crystal form 1 of Alpha1-antichymotrypsin variant DBS-II-allo: an allosterically modulated drug-binding serpin for doxorubicin Deposited 2018-02-22 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 26–383(358 aa)
Chain B 386–423(38 aa)
Mutation:L24R W194F W215Y E242Q K244N L269S P270Q K274S W276F R277F D278E A349R V355L K356E I357V T358L L359F L360Q Mutation:S361G A362P P382D T383N D384F Q386W N387S EDO 1,2-ETHANEDIOL × 3 DM2 DOXORUBICIN × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;293 K;0.2 M sodium thiocyanate, 20 % w/v PEG 3350
Resolution 1.80 Å R-free 0.221
6HGD Crystal structure of Alpha1-antichymotrypsin variant NewBG-0: a new binding globulin variant that is devoid of any cortisol-binding capabilities Deposited 2018-08-23 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 26–383(358 aa)
Chain B 384–423(40 aa)
Mutation:L24R, E242Q, K244N, K274N, R277G Mutation:P382D, T383H, D384F, Q386W No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;293 K;0.2 M magnesium chloride hexahydrate, 0.1 M BIS-Tris pH 6.5, 25 % w/v PEG 3350
Resolution 1.90 Å R-free 0.198
6HGE Crystal structure of Alpha1-antichymotrypsin variant NewBG-I in the uncleaved S-conformation Deposited 2018-08-23 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain A 26–423(398 aa)
Mutation:L24R, E242Q, K244N, L269S, P270R, K274N, R277G, P382D, T383H, D384F, Q386W, N387S Non-standard monomer:Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;293 K;0.2 M NaCl, 0.1 M Tris-HCl, pH 8.5, 25 % PEG 3350 supplemented with 10 % of a 0.5 M NaF solution, and additional 0.1 ul of a silver bullets bio reagent mixture consisting of thymidine, adenosine 3,5-cyclic monophosphate sodium salt monohydrate, sarcosine, 4-aminobenzoic acid, acarbose, inosine, 0.02 M HEPES sodium pH 6.8
Resolution 2.80 Å R-free 0.262
6HGE Crystal structure of Alpha1-antichymotrypsin variant NewBG-I in the uncleaved S-conformation Deposited 2018-08-23 Assembly 2 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain B 26–423(398 aa)
Mutation:L24R, E242Q, K244N, L269S, P270R, K274N, R277G, P382D, T383H, D384F, Q386W, N387S Non-standard monomer:Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;293 K;0.2 M NaCl, 0.1 M Tris-HCl, pH 8.5, 25 % PEG 3350 supplemented with 10 % of a 0.5 M NaF solution, and additional 0.1 ul of a silver bullets bio reagent mixture consisting of thymidine, adenosine 3,5-cyclic monophosphate sodium salt monohydrate, sarcosine, 4-aminobenzoic acid, acarbose, inosine, 0.02 M HEPES sodium pH 6.8
Resolution 2.80 Å R-free 0.262
6HGE Crystal structure of Alpha1-antichymotrypsin variant NewBG-I in the uncleaved S-conformation Deposited 2018-08-23 Assembly 3 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain C 26–423(398 aa)
Mutation:L24R, E242Q, K244N, L269S, P270R, K274N, R277G, P382D, T383H, D384F, Q386W, N387S Non-standard monomer:Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;293 K;0.2 M NaCl, 0.1 M Tris-HCl, pH 8.5, 25 % PEG 3350 supplemented with 10 % of a 0.5 M NaF solution, and additional 0.1 ul of a silver bullets bio reagent mixture consisting of thymidine, adenosine 3,5-cyclic monophosphate sodium salt monohydrate, sarcosine, 4-aminobenzoic acid, acarbose, inosine, 0.02 M HEPES sodium pH 6.8
Resolution 2.80 Å R-free 0.262
6HGE Crystal structure of Alpha1-antichymotrypsin variant NewBG-I in the uncleaved S-conformation Deposited 2018-08-23 Assembly 4 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain D 26–423(398 aa)
Mutation:L24R, E242Q, K244N, L269S, P270R, K274N, R277G, P382D, T383H, D384F, Q386W, N387S Non-standard monomer:Yes (specific site not provided by mmCIF) No recorded non-water small molecule X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;293 K;0.2 M NaCl, 0.1 M Tris-HCl, pH 8.5, 25 % PEG 3350 supplemented with 10 % of a 0.5 M NaF solution, and additional 0.1 ul of a silver bullets bio reagent mixture consisting of thymidine, adenosine 3,5-cyclic monophosphate sodium salt monohydrate, sarcosine, 4-aminobenzoic acid, acarbose, inosine, 0.02 M HEPES sodium pH 6.8
Resolution 2.80 Å R-free 0.262
6HGF Crystal structure of Alpha1-antichymotrypsin variant NewBG-II: a new binding globulin in complex with cortisol Deposited 2018-08-23 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 26–383(358 aa)
Chain B 384–423(40 aa)
Mutation:L24R, E242Q, K244N, L269S, P270R, K274A, R277G Mutation:P382D, T383H, D384F, Q386W, N387S EDO 1,2-ETHANEDIOL × 2 HCY (11alpha,14beta)-11,17,21-trihydroxypregn-4-ene-3,20-dione × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;293 K;0.2 M ammonium sulfate, 20 % w/v PEG 3350
Resolution 1.65 Å R-free 0.187
6HGG Crystal structure of Alpha1-antichymotrypsin variant NewBG-III: a new binding globulin in complex with cortisol Deposited 2018-08-23 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 26–383(358 aa)
Chain B 384–423(40 aa)
Mutation:L24R, L55V, E242Q, K244N, A251V, L252F, L269S, P270R, K274A, R277G Mutation:P382D, T383H, D384F, Q386W, N387S HCY (11alpha,14beta)-11,17,21-trihydroxypregn-4-ene-3,20-dione × 1 EDO 1,2-ETHANEDIOL × 5 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;293 K;2 % v/v Tacsimate pH 5.0, 0.1 M sodium citrate tribasic dihydrate pH 5.6, 16 % w/v PEG 3350
Resolution 1.79 Å R-free 0.216
6HGH Crystal structure of Alpha1-antichymotrypsin variant NewBG-III: a new binding globulin without any bound ligand Deposited 2018-08-23 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 26–383(358 aa)
Chain B 384–423(40 aa)
Mutation:L24R, L55V, E242Q, K244N, A251V, L252F, L269S, P270R, K274A, R277G Mutation:P382D, T383H, D384F, Q386W, N387S MLA MALONIC ACID × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;293 K;4 % Tacsimate pH 4.0, 12 % w/v PEG 3350
Resolution 1.90 Å R-free 0.240
6HGI Crystal structure of Alpha1-antichymotrypsin variant NewBG-III: a new binding globulin in complex with corticosterone Deposited 2018-08-23 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 26–383(358 aa)
Chain B 384–423(40 aa)
Mutation:L24R, L55V, E242Q, K244N, A251V, L252F, L269S, P270R, K274A, R277G Mutation:P382D, T383H, D384F, Q386W, N387S C0R CORTICOSTERONE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;293 K;2 % v/v Tacsimate pH 5.0, 0.1 M sodium citrate tribasic dihydrate pH 5.6, 16 % w/v PEG 3350
Resolution 1.52 Å R-free 0.193
6HGJ Crystal structure of Alpha1-antichymotrypsin variant NewBG-III: a new binding globulin in complex with aldosterone Deposited 2018-08-23 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 26–383(358 aa)
Chain B 384–423(40 aa)
Mutation:L24R, L55V, E242Q, K244N, A251V, L252F, L269S, P270R, K274A, R277G Mutation:P382D, T383H, D384F, Q386W, N387S AS4 ALDOSTERONE × 1 EDO 1,2-ETHANEDIOL × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;292 K;2 % v/v Tacsimate pH 5.0, 0.1 M sodium citrate tribasic dihydrate pH 5.6, 16 % w/v PEG 3350
Resolution 1.82 Å R-free 0.221
6HGK Crystal structure of Alpha1-antichymotrypsin variant NewBG-III: a new binding globulin in complex with progesterone Deposited 2018-08-23 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 26–383(358 aa)
Chain B 384–423(40 aa)
Mutation:L24R, L55V, E242Q, K244N, A251V, L252F, L269S, P270R, K274A, R277G Mutation:P382D, T383H, D384F, Q386W, N387S STR PROGESTERONE × 1 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;293 K;2 % Tacsimate pH 6.0, 0.1 M BIS-Tris pH 6.5, 20 % w/v PEG 3350
Resolution 1.85 Å R-free 0.227
6HGL Crystal structure of Alpha1-antichymotrypsin variant NewBG-III: a new binding globulin in complex with testosterone Deposited 2018-08-23 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 26–383(358 aa)
Chain B 384–423(40 aa)
Mutation:L24R, L55V, E242Q, K244N, A251V, L252F, L269S, P270R, K274A, R277G Mutation:P382D, T383H, D384F, Q386W, N387S TES TESTOSTERONE × 1 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;293 K;2 % v/v Tacsimate pH 5.0, 0.1 M sodium citrate tribasic dihydrate pH 5.6, 16 % w/v PEG 3350
Resolution 1.92 Å R-free 0.224
6HGM Crystal structure of Alpha1-antichymotrypsin variant NewBG-III-allo: an allosterically controlled new binding globulin with an unprecedentedly high ligand release efficacy Deposited 2018-08-23 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 26–383(358 aa)
Chain B 384–423(40 aa)
Mutation:L24R, L55V, E242Q, K244N, A251V, L252F, L269S, P270R, K274A, R277G, A349R Mutation:P382D, T383H, D384F, Q386W, N387S CL CHLORIDE ION × 3 CA CALCIUM ION × 3 EDO 1,2-ETHANEDIOL × 2 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, HANGING DROP;293 K;0.3 M calcium chloride dihydrate, 20 % w/v PEG 3350
Resolution 1.37 Å R-free 0.181
6HGN Crystal structure of Alpha1-antichymotrypsin variant DBS-II-allo-L55V: an allosterically controlled doxorubicin-binding serpin with an unprecedentedly high ligand release efficacy Deposited 2018-08-23 Assembly 1 Protein homooligomer Homooligomer;Protein × 2 PDB declaration: dimeric(2) Consistent with protein count
Chain A 26–383(358 aa)
Chain B 384–423(40 aa)
Mutation:L24R, L55V, W194F,W215Y, E242Q, K244N, L269S, P270Q, K274S, W276F, R277F, D278E, A349R, V355L, K356E, I357V, T358L, L359F, L360Q Mutation:S361G, A362P, P382D, T383N, D384F, Q386W, N387S EDO 1,2-ETHANEDIOL × 4 X-RAY DIFFRACTION
X-ray crystallization conditions VAPOR DIFFUSION, SITTING DROP;293 K;2 % Tacsimate pH 4.0, 0.1 M Sodium acetate trihydrate pH 4.6, 16 % w/v PEG 3,350
Resolution 1.48 Å R-free 0.199
9C2T Infectious B19V capsid Deposited 2024-05-31 Assembly 1 Protein heterocomplex Heteromer;Protein × 7 PDB declaration: heptameric(7) Consistent with protein count
Chain S 48–422(375 aa)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.10 Å
9D7K Infectious B19V capsid Deposited 2024-08-16 Assembly 1 Protein monomer Monomer;Protein × 1 PDB declaration: monomeric(1) Consistent with protein count
Chain S 1–423(423 aa)
Not recorded No recorded non-water small molecule ELECTRON MICROSCOPY
cryo-EM buffer pH 7
cryo-EM vitrification conditions Cryogen ETHANE
Resolution 3.00 Å